Multiblock Bioadhesive Hydrogel With Wet Adhesion and pH Response
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Solution Overview
Problem
Existing bioadhesive materials lack sufficient stimulus responsiveness and adhesion strength, particularly under wet conditions, limiting their applications in biomedical fields such as drug carriers and tissue engineering.
Innovation Solution
A multiblock copolypeptide is developed by fusing adhesive elastin-based polypeptides (EBP) and suckerin-based polypeptides (SBP), with tyrosine residues modified to 3,4-dihydroxyphenylalanine (DOPA) to enhance adhesion, forming self-assembled nanostructures and hydrogels that respond to temperature and pH stimuli.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Strength
If bioadhesive materials are designed to provide strong adhesion, then adhesion strength is improved, but stimulus responsiveness deteriorates
Solution Approach 1:
The patent combines elastin-based polypeptides (providing stimulus responsiveness through temperature-induced phase transition) with suckerin-based polypeptides (providing adhesion through DOPA and lysine residues) into a single multiblock copolypeptide structure. This merging allows the material to simultaneously exhibit both strong adhesion and stimulus responsiveness, resolving the contradiction between these two properties.
Solution Approach 2:
The invention creates a composite polypeptide material integrating two distinct functional domains: elastin-like polypeptide blocks for thermoresponsiveness and suckerin-like polypeptide blocks for adhesion. The multiblock architecture allows each domain to contribute its inherent properties, achieving a composite material that exhibits both strong adhesion and stimulus responsiveness.
2Strength
If adhesion proteins use DOPA for surface adhesion, then adhesion strength is improved, but adhesion under wet conditions deteriorates
Solution Approach 1:
The patent merges DOPA-containing suckerin blocks (for adhesion) with elastin-based blocks (for hydrophobic interactions and water resistance) into a multiblock copolypeptide. The elastin blocks provide a hydrophobic environment that protects the DOPA adhesion sites from water interference, allowing strong adhesion to persist under wet conditions.
Solution Approach 2:
The multiblock structure creates local functional zones: DOPA-rich regions for adhesion and elastin-rich regions for hydrophobic protection. This local quality differentiation allows the adhesion sites to maintain their binding capability while being shielded from water by the hydrophobic elastin domains, resolving the contradiction between adhesion strength and wet condition reliability.
3Stability of the object's composition
If multiblock copolypeptide is designed for self-assembly, then structural organization is improved, but manufacturing complexity deteriorates
Solution Approach 1:
The multiblock copolypeptide is designed with intrinsic self-assembly capability through its amphiphilic structure and block composition. The polymer automatically organizes into micelles or hydrogels in aqueous solutions without requiring external assembly equipment or complex processing steps. This self-service approach improves structural organization while minimizing manufacturing complexity.
Solution Approach 2:
The self-assembly behavior is controlled by changing simple parameters such as temperature (triggering elastin phase transition) and pH (affecting DOPA adhesion). These parameter changes drive spontaneous self-organization of the copolypeptide into functional structures, achieving high structural organization through simple parameter control rather than complex manufacturing processes.
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The multiblock copolypeptide exhibits strong surface adhesion and reversible changes under wet conditions, making it suitable for drug carriers, biocoating agents, and bioadhesives with improved performance in biomedical applications.
Implementation Method 1
Multiple pentapeptide repeating units Val/Ile-Pro-Gly/Ala-Xaa-Gly (SEQ ID NO:14) undergo a reversible reverse phase transition at a lower critical solution temperature (LCST), i.e., the transition temperature (Tt)
Implementation Method 2
These adhesion proteins inspired by the adhesion of mussels under harsh and humid conditions all have 3,4-dihydroxyphenylalanine (DOPA) as a hydroxylated form of tyrosine (Y) to adhere to the surface through various interactions between DOPA molecules and adhesion surface molecules
Implementation Method 3
increases adhesion through interaction between lysine (K) and 7-cation
Implementation Method 4
An A1H1 sequence (peptide sequence AATAVSHTTHHA (SEQ ID NO:12) of the module M1), which is mainly found in the suckerin protein family, is self-assembled similarly to a crystal structure in an aqueous solution, and a β-sheet distance is 4.4 and 5.4 Å to form very dense self-assembled nanocrystals. These β-sheet nanocrystals serve as physical and reversible cross-linking through hydrogen bonding
Data Source
AI summary
The present disclosure relates to an adhesive elastin and suckerin-based multiblock copolypeptide with stimulus responsiveness and surface adhesion, a self-assembled structure thereof, and application of an injectable hydrogel as a bioadhesive.